ArticleThe Journal of biological chemistry2012
Structural characterization and oligomerization of the TssL protein, a component shared by bacterial type VI and type IVb secretion systems.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 89 citations in OpenAlex.
- The type VI secretion system and associated effector proteins.Nature reviews. Microbiology · 2026Review
- Transmembrane effector substrates of type IV secretion systems: mechanisms of secretion and insertion into host cell membranes.microLife · 2026Review
- The Competitive Edge: T6SS-Mediated Interference Competition byMicroorganisms · 2025Review
- Transcriptome profiling of type VI secretion system core geneMicrobiology spectrum · 2024Article
- Bacterial One- and Two-Hybrid Assays to Monitor Transmembrane Helix Interactions.Methods in molecular biology (Clifton, N.J.) · 2024Article
- AlignScape, displaying sequence similarity using self-organizing maps.Frontiers in bioinformatics · 2024Article
- Pathogenicity and virulence ofVirulence · 2023Review
- Structure and Function of the Dot/Icm T4SS.bioRxiv : the preprint server for biology · 2023Article
- Bacterial type VI secretion system (T6SS): an evolved molecular weapon with diverse functionality.Biotechnology letters · 2023Review
- The type-VI secretion system of the beneficial symbiontMicrobiology (Reading, England) · 2023Review
- The Missing Pieces: The Role of Secretion Systems inBiomolecules · 2023Review
- Type VI Secretion Systems: Environmental and Intra-host Competition of Vibrio cholerae.Advances in experimental medicine and biology · 2023Article
- Subcellular localization of Type VI secretion system assembly in response to cell-cell contact.The EMBO journal · 2022Article
- Klebsiella pneumoniae induces host metabolic stress that promotes tolerance to pulmonary infection.Cell metabolism · 2022Article
- Recent advances in structural studies of the Legionella pneumophila Dot/Icm type IV secretion system.Microbiology and immunology · 2022Review
- Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.PloS one · 2021Article
- Two Signal Recognition Particle Sequences Are Present in the Amino-Terminal Domain of the C-Tailed Protein SciP.Journal of bacteriology · 2020Article
- Structural Characterization of TssL from Acinetobacter baumannii: a Key Component of the Type VI Secretion System.Journal of bacteriology · 2020Article
- ClpV3 of the H3-Type VI Secretion System (H3-T6SS) Affects Multiple Virulence Factors inFrontiers in microbiology · 2020Article
- Solving the Puzzle: Connecting a HeterologousFrontiers in cellular and infection microbiology · 2020Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Type VI secretion system (T6SS) is a macromolecular system distributed in Gram-negative bacteria, responsible for the secretion of effector proteins into target cells. The T6SS has a broad versatility as it can target both eukaryotic and prokaryotic cells. It is therefore involved in host pathogenesis or killing neighboring bacterial cells to colonize a new niche. At the architecture level, the T6SS core apparatus is composed of 13 proteins, which assemble in two subcomplexes. One of these subcomplexes, composed of subunits that share structural similarities with bacteriophage tail and baseplate components, is anchored to the cell envelope by the membrane subcomplex. This latter is constituted of at least three proteins, TssL, TssM, and TssJ. The crystal structure of the TssJ outer membrane lipoprotein and its interaction with the inner membrane TssM protein have been recently reported. TssL and TssM share sequence homology and characteristics with two components of the Type IVb secretion system (T4bSS), IcmH/DotU and IcmF, respectively. In this study, we report the crystal structure of the cytoplasmic domain of the TssL inner membrane protein from the enteroaggregative Escherichia coli Sci-1 T6SS. It folds as a hook-like structure composed of two three-helix bundles. Two TssL molecules associate to form a functional complex. Although the TssL trans-membrane segment is the main determinant of self-interaction, contacts between the cytoplasmic domains are required for TssL function. Based on sequence homology and secondary structure prediction, we propose that the TssL structure is the prototype for the members of the TssL and IcmH/DotU families.
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